Inhibition of Epstein-Barr virus OriP function by tankyrase, a telomere-associated poly-ADP ribose polymerase that binds and modifies EBNA1 - Wikidata - wikimedia - TriplyDB

Inhibition of Epstein-Barr virus OriP function by tankyrase, a telomere-associated poly-ADP ribose polymerase that binds and modifies EBNA1

Inhibition of Epstein-Barr virus OriP function by tankyrase, a telomere-associated poly-ADP ribose polymerase that binds and modifies EBNA1

http://www.wikidata.org/entity/Q24520598

about

EBNA1-mediated recruitment of a histone H2B deubiquitylating complex to the Epstein-Barr virus latent origin of DNA replication Rickettsia Phylogenomics: Unwinding the Intricacies of Obligate Intracellular Life para-Substituted 2-phenyl-3,4-dihydroquinazolin-4-ones as potent and selective tankyrase inhibitors Genome-wide association analysis of susceptibility and clinical phenotype in multiple sclerosis A role for the nucleosome assembly proteins TAF-Iβ and NAP1 in the activation of BZLF1 expression and Epstein-Barr virus reactivation Regulation of Epstein-Barr virus OriP replication by poly(ADP-ribose) polymerase 1.PARP1 promotes nucleotide excision repair through DDB2 stabilization and recruitment of ALC1 Regulation of the EBNA1 Epstein-Barr virus protein by serine phosphorylation and arginine methylation Scaffold hopping approach on the route to selective tankyrase inhibitors.Post-Translational Modifications of Kaposi's Sarcoma-Associated Herpesvirus Regulatory Proteins - SUMO and KSHV The telomeric PARP, tankyrases, as targets for cancer therapy Telomeres and viruses: common themes of genome maintenance.The plasmid replicon of Epstein-Barr virus: mechanistic insights into efficient, licensed, extrachromosomal replication in human cells.The EBNA1 protein of Epstein-Barr virus functionally interacts with Brd4 Proteome-wide identification of poly(ADP-ribose) binding proteins and poly(ADP-ribose)-associated protein complexes.Regulation and dysregulation of Epstein-Barr virus latency: implications for the development of autoimmune diseases.Epigenetic regulation of EBV and KSHV latency Tankyrases as drug targets.The origin recognition complex in human diseases.The Epstein-Barr Virus EBNA1 Protein.Tankyrases: structure, function and therapeutic implications in cancer.At a crossroads: human DNA tumor viruses and the host DNA damage response.Nucleosome assembly proteins bind to Epstein-Barr virus nuclear antigen 1 and affect its functions in DNA replication and transcriptional activation.Regulation of Telomere Homeostasis during Epstein-Barr virus Infection and Immortalization.Carcinoma-risk variant of EBNA1 deregulates Epstein-Barr Virus episomal latency.Functions of the Epstein-Barr virus EBNA1 protein in viral reactivation and lytic infection.

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Inhibition of Epstein-Barr virus OriP function by tankyrase, a telomere-associated poly-ADP ribose polymerase that binds and modifies EBNA1

http://www.wikidata.org/entity/Q24520598

description

2005 nî lūn-bûn

@nan

2005 թուականի Ապրիլին հրատարակուած գիտական յօդուած

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2005 թվականի ապրիլին հրատարակված գիտական հոդված

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2005年の論文

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2005年論文

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2005年論文

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2005年論文

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2005年論文

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2005年論文

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2005年论文

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name

Inhibition of Epstein-Barr vir ...... that binds and modifies EBNA1

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Inhibition of Epstein-Barr vir ...... that binds and modifies EBNA1

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Inhibition of Epstein-Barr vir ...... that binds and modifies EBNA1

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Inhibition of Epstein-Barr vir ...... that binds and modifies EBNA1

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Inhibition of Epstein-Barr vir ...... that binds and modifies EBNA1

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Inhibition of Epstein-Barr vir ...... that binds and modifies EBNA1

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Inhibition of Epstein-Barr vir ...... that binds and modifies EBNA1

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Inhibition of Epstein-Barr vir ...... that binds and modifies EBNA1

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Inhibition of Epstein-Barr vir ...... that binds and modifies EBNA1

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Inhibition of Epstein-Barr vir ...... that binds and modifies EBNA1

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JVI.79.8.4640-4650.2005

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Journal of Virology

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Inhibition of Epstein-Barr vir ...... that binds and modifies EBNA1

@en

P2093

Constandache Atanasiu

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Juan I Sbodio

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Kehao Zhao

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Nai-Wen Chi

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Paul M Lieberman

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Ronen Marmorstein

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Zhong Deng

http://www.w3.org/2001/XMLSchema#string

P2860

Tankyrase, a poly(ADP-ribose) polymerase at human telomeres

TANK2, a new TRF1-associated poly(ADP-ribose) polymerase, causes rapid induction of cell death upon overexpression

The telomeric poly(ADP-ribose) polymerase, tankyrase 1, contains multiple binding sites for telomeric repeat binding factor 1 (TRF1) and a novel acceptor, 182-kDa tankyrase-binding protein (TAB182)

TRF1 is a dimer and bends telomeric DNA

EBP2, a human protein that interacts with sequences of the Epstein-Barr virus nuclear antigen 1 important for plasmid maintenance.

Tankyrase-2 oligomerizes with tankyrase-1 and binds to both TRF1 (telomere-repeat-binding factor 1) and IRAP (insulin-responsive aminopeptidase)

The EBV nuclear antigen 1 (EBNA1) enhances B cell immortalization several thousandfold

TRF1 is degraded by ubiquitin-mediated proteolysis after release from telomeres

Tankyrase is a golgi-associated mitogen-activated protein kinase substrate that interacts with IRAP in GLUT4 vesicles

Cell cycle dependent localization of the telomeric PARP, tankyrase, to nuclear pore complexes and centrosomes

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scholarly article

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10.1128/JVI.79.8.4640-4650.2005

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8

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79

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Ronen Marmorstein

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2005-04-01T00:00:00Z

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7941208

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15795250

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Epstein–Barr virus

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1069541

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